Elucidating the Impact of Payload Conjugation on the Cell-Penetrating Efficiency of the Endosomal Escape Peptide dfTAT: Implications for Future Designs for CPP-Based Delivery Systems
Author:
Affiliation:
1. Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, United States
2. Department of Chemistry, Texas A&M University, College Station, Texas 77843, United States
Funder
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Organic Chemistry,Pharmaceutical Science,Pharmacology,Biomedical Engineering,Bioengineering,Biotechnology
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.bioconjchem.3c00369
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1. Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein
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3. Identification of a novel cell attachment domain in the HIV-1 Tat protein and its 90-kDa cell surface binding protein.
4. Cell penetrating peptides: the potent multi-cargo intracellular carriers
5. Enhanced Delivery of Synthetic Labelled Ubiquitin into Live Cells by Using Next‐Generation Ub–TAT Conjugates
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